1-Naphthyl acetate: A chromogenic substrate for the detection of erythrocyte acetylcholinesterase activity

Biochimie ◽  
2018 ◽  
Vol 154 ◽  
pp. 194-209 ◽  
Author(s):  
Sheemona Chowdhary ◽  
Rajasri Bhattacharyya ◽  
Dibyajyoti Banerjee
Keyword(s):  
Acetylcholinesterase Activity ◽  
Chromogenic Substrate ◽  
Naphthyl Acetate

scholarly journals The Role of Acetylcholine Esterase in Resistance Mechanism of Plutella xylostella to Emamektin Benzoate

2018 ◽  
Vol 10 (1) ◽  
pp. 66-71
Author(s):  
Udi Tarwotjo ◽  
Rully Rahadian
Keyword(s):  
Enzyme Activity ◽  
Esterase Activity ◽  
Resistance Mechanism ◽  
Acetylcholinesterase Activity ◽  
Acetylcholine Esterase ◽  
Emamectin Benzoate ◽  
Susceptible Population ◽  
The Third ◽  
Naphthyl Acetate

One of the resistance mechanism of P. xylostellato emamektin benzoate is target insensitivity which is acetylcholine esterase that responsible for resistance occurrence. The objective of this study was to determine the role of acetylcholinesterase in the resistance mechanism of P. xylostella population to emamektin benzoate. For enzyme activity analysis, larvae homogenate of the third instar of P. xylostella was prepared. The number of insects required for each scour is 1 for each field population. The protein content in P. xylostella homogenate was measured by the Folin-Ciocalteu test. Non-specific esterase activity with an absorption rate was read using ELISA reader tool with λ = 450 nm. The inhibition level of acetylcholinesterase activity by emamectin benzoate in the tested population was 36.84%. The highest inhibition occurs in Puasan (Ngablak) population.  The result shows that a α-naphthyl acetate substrate was used so that it was recorded as non-specific esterase activity and did not exhibit esterase activity which specifically describes emamectin benzoate. Non-specific esterase enzyme activity of either α or β-naphthyl acetate substances to benzoic emamectin in the tested population most of the population was still susceptible. On α-naphthyl acetate substrate, the highest absorbance value found in susceptible population to benzoate emamectin (0.773), while the lowest found in Babrik (Ngablak) population  (0.083).

scholarly journals DISTRIBUTION OF ESTERASES IN THE MYONEURAL JUNCTION OF THE STRIATED MUSCLE OF THE RAT

1967 ◽  
Vol 15 (7) ◽  
pp. 399-403 ◽  
Author(s):  
O. ERÄNKÖ ◽  
H. TERÄVÄINEN
Keyword(s):  
Esterase Activity ◽  
Striated Muscle ◽  
Acetylcholinesterase Activity ◽  
Nonspecific Esterase ◽  
Selective Inhibitors ◽  
Myoneural Junction ◽  
Terminal Axon ◽  
Naphthyl Acetate ◽  
Nonspecific Esterase Activity

Distribution of esterases in the myoneural junction of the striated muscle of the rat was studied using acetylthiocholine, butyrylthiochobine and α-naphthyl acetate as substrates, together with selective inhibitors. Acetylcholinesterase activity was observed in the peripheral complex of synaptic folds. Nonspecific cholinesterase was detected in the peripheral complex of synaptic folds and the teloglia with approximately equal activities. Nonspecific esterase activity, present in tissues incubated with eserine, was marked in the terminal axon and was also present in the teloglia and synaptic folds.

Chemically Contaminated Eel Fed to Pregnant and Lactating Mouse Dams Causes Hyperactivity in Their Offspring

2016 ◽  
Vol 86 (1-2) ◽  
pp. 36-47 ◽  
Author(s):  
Imen Dridi ◽  
Nidhal Soualeh ◽  
Torsten Bohn ◽  
Rachid Soulimani ◽  
Jaouad Bouayed
Keyword(s):  
Open Field ◽  
Early Life ◽  
Home Cage ◽  
Anguilla Anguilla ◽  
Acetylcholinesterase Activity ◽  
Female Offspring ◽  
Significant Inhibition ◽  
Standard Diet ◽  
Early Life Exposure ◽  
Cage Test

Abstract.This study examined whether perinatal exposure to polluted eels (Anguilla anguilla L.) induces changes in the locomotor activity of offspring mice across lifespan (post-natal days (PNDs) 47 – 329), using the open field and the home cage activity tests. Dams were exposed during gestation and lactation, through diets enriched in eels naturally contaminated with pollutants including PCBs. Analysis of the eel muscle focused on the six non-dioxin-like (NDL) indicator PCBs (Σ6 NDL-PCBs: 28, 52, 101, 138, 153 and 180). Four groups of dams (n = 10 per group) received either a standard diet without eels or eels (0.8 mg/kg/day) containing 85, 216, or 400 ng/kg/day of ϵ6 NDL-PCBs. The open field test showed that early-life exposure to polluted eels increased locomotion in female offspring of exposed dams but not in males, compared to controls. This hyperlocomotion appeared later in life, at PNDs 195 and 329 (up to 32 % increase, p < 0.05). In addition, overactivity was observed in the home cage test at PND 305: exposed offspring females showed a faster overall locomotion speed (3.6 – 4.2 cm/s) than controls (2.9 cm/s, p <0.05); again, males remained unaffected. Covered distances in the home cage test were only elevated significantly in offspring females exposed to highest PCB concentrations (3411 ± 590 cm vs. 1377 ± 114 cm, p < 0.001). These results suggest that early-life exposure to polluted eels containing dietary contaminants including PCBs caused late, persistent and gender-dependent neurobehavioral hyperactive effects in offspring mice. Furthermore, female hyperactivity was associated with a significant inhibition of acetylcholinesterase activity in the hippocampus and the prefrontal cortex.

Normal phase HPLC profiling of the acetylcholinesterase activity in apolar plant extracts

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
A Landreau ◽  
S Bertrand ◽  
C Simoes-Pires ◽  
L Marcourt ◽  
TD Bach ◽  
...  
Keyword(s):  
Plant Extracts ◽  
Acetylcholinesterase Activity ◽  
Normal Phase ◽  
Normal Phase Hplc

Factor XII Determinations in the Presence and Absence of Phospholipid Antibodies

1998 ◽  
Vol 79 (01) ◽  
pp. 87-90 ◽  
Author(s):  
D. W. Jones ◽  
M. Winter ◽  
M. J. Gallimore
Keyword(s):  
Lower Limit ◽  
Lupus Anticoagulant ◽  
Factor Xii ◽  
Chromogenic Substrate ◽  
Plasma Samples ◽  
Presence And Absence ◽  
Lower Limit Of Normal

SummaryFactor XII (FXII) levels were determined in plasma samples from 29 normal donors, 10 patients with inherited FXII deficiency (all lupus anticoagulant [LA] negative) and 67 LA positive patients, using clotting (FXIIct), chromogenic substrate (FXIIcs) and immunochemical (FXIIag) assays. Excellent correlations were obtained in the three FXII assays with the LA negative samples and between the FXIIcs and FXIIag assays in the LA positive samples. Correlations between both the FXIIcs and FXIIag with FXIIct in the LA positive patients were poor. Of 67 LA positive samples studied, 25 (37.3%) showed lower values in the FXIIct assay; 13 (19.4%) of these patients were pseudo FXII deficient with values of FXII below the lower limit of normal.These results indicate that a diagnosis of FXII deficiency can be made inappropriately in the presence of phospholipid antibodies and that such a diagnosis should not be made by FXIIct assay alone.

Visualization of von Willebrand Factor Multimers by Enzyme-Conjugated Secondary Antibodies

1986 ◽  
Vol 55 (02) ◽  
pp. 276-278 ◽  
Author(s):  
F Brosstad ◽  
Inge Kjønniksen ◽  
B Rønning ◽  
H Stormorken
Keyword(s):  
Von Willebrand Factor ◽  
Chromogenic Substrate ◽  
Agarose Electrophoresis ◽  
Secondary Antibodies ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Beta Galactosidase

SummaryA method for visualization of the multimeric forms of von Willebrand Factor (vWF) in plasma and platelets is described. The method is based upon: 1) Separation of the vWF multimers by SDS-agarose electrophoresis, 2) Subsequent blotting of the vWF multimers onto nitrocellulose, 3) Immunolocalization and visualization of the vWF pattern by the sequential incubation of the blot with a) primary vWF antiserum, b) peroxidase- or beta-galactosidase-conjugated secondary antibodies and a relevant chromogenic substrate.

Plasma Thrombin Assay using a Chromogenic Substrate in Disseminated Intravascular Coagulation due to Snake Bite Envenomation

1979 ◽  
Vol 41 (03) ◽  
pp. 544-552 ◽  
Author(s):  
R P Herrmann ◽  
P E Bailey
Keyword(s):  
Disseminated Intravascular Coagulation ◽  
Degradation Products ◽  
Snake Bite ◽  
Chromogenic Substrate ◽  
Coagulation Parameters ◽  
Fibrinogen Degradation Products ◽  
Intravascular Coagulation

SummaryUsing the chromogenic substrate, Tos-Gly-Pro-Arg-pNA-HCL (Chromozym TH, Boehringer Mannheim) plasma thrombin was estimated in six cases of envenomation by Australian elapid snakes. All patients manifested findings chracteristic of defibrination due to envenomation by these snakes. Fibrin-fibrinogen degradation products were grossly elevated, as was plasma thrombin in all cases.Following treatment with antivenene, all abnormal coagulation parameters returned rapidly towards normal by 24 hours and plasma thrombin disappeared.

Amidolytic Detection of Prothrombin Activation Products after SDS-Gel Electrophoresis

1989 ◽  
Vol 61 (03) ◽  
pp. 386-391 ◽  
Author(s):  
Guido Tans ◽  
Truus Janssen-Claessen ◽  
Jan Rosing
Keyword(s):  
Gel Electrophoresis ◽  
Activated Protein C ◽  
Factor Xa ◽  
Coagulation Factors ◽  
Product Formation ◽  
Chromogenic Substrate ◽  
Nitrocellulose Membrane ◽  
Activation Products ◽  
Factor Xia ◽  
Prothrombin Activation

SummaryIn this paper we report a method via which enzymatically active products formed during prothrombin activation can be detected by simple photographic means after SDS-gel electrophoresis, blotting onto a nitrocellulose membrane and visualization with the chromogenic substrate, S2238. After amidolytic detection the same nitrocellulose membrane can also be used for immunologic detection of prothrombin activation products, thus allowing a complete description of product formation during prothrombin activation.The detection limit of the so-called “amidoblot” is approximately 3 ng thrombin per gel sample which is comparable to the sensitivity of immunoblotting.It is further shown that the amidoblot technique can also be applied to other coagulation factors for which a suitable chromogenic substrate is available (factor XIIa, kallikrein, factor XIa, factor Xa, plasmin and activated protein C).

Aggregated, Conformationally Changed Fibrinogen Exposes the Stimulating Sites for t-PA-Catalysed Plasminogen Activation

1996 ◽  
Vol 75 (02) ◽  
pp. 326-331 ◽  
Author(s):  
Unni Haddeland ◽  
Knut Sletten ◽  
Anne Bennick ◽  
Willem Nieuwenhuizen ◽  
Frank Brosstad
Keyword(s):  
Conformational Changes ◽  
Gel Permeation Chromatography ◽  
Tissue Type ◽  
Plasminogen Activation ◽  
Chromogenic Substrate ◽  
Type Plasminogen Activator ◽  
Gel Permeation ◽  
Self Association ◽  
Fibrin Monomers ◽  
Stimulation Of

SummaryThe present paper shows that conformationally changed fibrinogen can expose the sites Aα-(148-160) and γ-(312-324) involved in stimulation of the tissue-type plasminogen activator (t-PA)-catalysed plasminogen activation. The exposure of the stimulating sites was determined by ELISA using mABs directed to these sites, and was shown to coincide with stimulation of t-PA-catalysed plasminogen activation as assessed in an assay using a chromogenic substrate for plasmin. Gel permeation chromatography of fibrinogen conformationally changed by heat (46.5° C for 25 min) demonstrated the presence of both aggregated and monomeric fibrinogen. The aggregated fibrinogen, but not the monomeric fibrinogen, had exposed the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation. Fibrinogen subjected to heat in the presence of 3 mM of the tetrapeptide GPRP neither aggregates nor exposes the rate-enhancing sites. Thus, aggregation and exposure of t-PA-stimulating sites in fibrinogen seem to be related phenomena, and it is tempting to believe that the exposure of stimulating sites is a consequence of the conformational changes that occur during aggregation, or self-association. Fibrin monomers kept in a monomeric state by a final GPRP concentration of 3 mM do not expose the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation, whereas dilution of GPRP to a concentration that is no longer anti-polymerizing, results in exposure of these sites. Consequently, the exposure of t-PA-stimulating sites in fibrin as well is due to the conformational changes that occur during selfassociation.

Lack of Agreement of Chromogenic and Glotting Assays for Factor X and Protein C in Warfarinised Plasma

1991 ◽  
Vol 65 (04) ◽  
pp. 360-363 ◽  
Author(s):  
P Han ◽  
K P Fung ◽  
U Rahdakrishnan
Keyword(s):  
Serine Proteases ◽  
Protein C ◽  
Warfarin Therapy ◽  
Intraclass Correlation ◽  
Chromogenic Substrate ◽  
Factor X ◽  
Laboratory Automation ◽  
Quantitative Results ◽  
Assay Methods

SummaryCoagulation serine proteases can be measured with either a chromogenic substrate assay or a clotting assay using deficient plasmas. It is a concern whether both assays give similar quantitative results, in particular in plasma obtained fiom patients on long term warfarin therapy. If these two assay methods were interchangeable, then the chromogenic substrate assay has the advantages of precision as well as laboratory automation. We used the intraclass correlation coefficient (r1) to assess the agreement between the two methods in measuring factor X and protein C levels in warfarinised plasma. The results indicate that the extent and pattern of agreement of the two methods for the measurement of the two variables in warfarinised plasma are poor, despite high Pearson product moment coefficients of correlation.

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